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Protein

Histone H2A type 1

Gene
N/A
Organism
Xenopus laevis (African clawed frog)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.

GO - Molecular functioni

Keywordsi

Molecular functionDNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H2A type 1
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-6493983 h2afx

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Chromosome, Nucleosome core, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00000552942 – 130Histone H2A type 1Add BLAST129

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineBy similarity1
Modified residuei2PhosphoserineBy similarity1
Modified residuei6N6-(2-hydroxyisobutyryl)lysineBy similarity1
Modified residuei6N6-acetyllysineBy similarity1
Modified residuei10N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity1
Modified residuei10N6-succinyllysineBy similarity1
Cross-linki14Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki16Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei37N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity1
Modified residuei75N6-(2-hydroxyisobutyryl)lysineBy similarity1
Modified residuei76N6-(2-hydroxyisobutyryl)lysineBy similarity1
Modified residuei96N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity1
Modified residuei96N6-succinyllysineBy similarity1
Modified residuei105N5-methylglutamineBy similarity1
Modified residuei119N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity1
Cross-linki120Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity

Post-translational modificationi

Monoubiquitination of Lys-120 (H2AK119Ub) gives a specific tag for epigenetic transcriptional repression. Following DNA double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63' linkage of ubiquitin moieties, leading to the recruitment of repair proteins to sites of DNA damage. H2AK119Ub and ionizing radiation-induced 'Lys-63'-linked ubiquitination are distinct events (By similarity).By similarity
Phosphorylation on Ser-2 is enhanced during mitosis. Phosphorylation on Ser-2 directly represses transcription (By similarity).By similarity
Glutamine methylation at Gln-105 (H2AQ104me) by FBL is specifically dedicated to polymerase I. It is present at 35S ribosomal DNA locus and impairs binding of the FACT complex (By similarity).By similarity

Keywords - PTMi

Acetylation, Hydroxylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiP06897

Interactioni

Subunit structurei

The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA.

GO - Molecular functioni

Protein-protein interaction databases

BioGridi592527, 2 interactors
DIPiDIP-39144N
IntActiP06897, 10 interactors

Structurei

Secondary structure

1130
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP06897
SMRiP06897
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06897

Family & Domainsi

Sequence similaritiesi

Belongs to the histone H2A family.Curated

Phylogenomic databases

HOVERGENiHBG009342
KOiK11251

Family and domain databases

CDDicd00074 H2A, 1 hit
Gene3Di1.10.20.10, 1 hit
InterProiView protein in InterPro
IPR009072 Histone-fold
IPR002119 Histone_H2A
IPR007125 Histone_H2A/H2B/H3
IPR032454 Histone_H2A_C
IPR032458 Histone_H2A_CS
PfamiView protein in Pfam
PF00125 Histone, 1 hit
PF16211 Histone_H2A_C, 1 hit
PRINTSiPR00620 HISTONEH2A
SMARTiView protein in SMART
SM00414 H2A, 1 hit
SUPFAMiSSF47113 SSF47113, 1 hit
PROSITEiView protein in PROSITE
PS00046 HISTONE_H2A, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P06897-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSGRGKQGGK TRAKAKTRSS RAGLQFPVGR VHRLLRKGNY AERVGAGAPV
60 70 80 90 100
YLAAVLEYLT AEILELAGNA ARDNKKTRII PRHLQLAVRN DEELNKLLGG
110 120 130
VTIAQGGVLP NIQSVLLPKK TESAKSAKSK
Length:130
Mass (Da):13,966
Last modified:January 23, 2007 - v2
Checksum:i09946ABF27FA52A9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03018 Genomic DNA Translation: CAA26817.1
M21287 Genomic DNA Translation: AAA49769.1
BC106331 mRNA Translation: AAI06332.1
PIRiH24510 HSXLA1
RefSeqiNP_001089684.1, NM_001096215.1
UniGeneiXl.19141

Genome annotation databases

GeneIDi734746
KEGGixla:734746

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03018 Genomic DNA Translation: CAA26817.1
M21287 Genomic DNA Translation: AAA49769.1
BC106331 mRNA Translation: AAI06332.1
PIRiH24510 HSXLA1
RefSeqiNP_001089684.1, NM_001096215.1
UniGeneiXl.19141

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AOIX-ray2.80C/G5-120[»]
1KX3X-ray2.00C/G2-130[»]
1KX4X-ray2.60C/G2-130[»]
1KX5X-ray1.94C/G2-130[»]
1M18X-ray2.45C/G2-130[»]
1M19X-ray2.30C/G2-130[»]
1M1AX-ray2.65C/G2-130[»]
1P34X-ray2.70C/G2-130[»]
1P3AX-ray3.00C/G2-130[»]
1P3BX-ray3.00C/G2-130[»]
1P3FX-ray2.90C/G2-130[»]
1P3GX-ray2.70C/G2-130[»]
1P3IX-ray2.30C/G2-130[»]
1P3KX-ray2.90C/G2-130[»]
1P3LX-ray2.40C/G2-130[»]
1P3MX-ray2.90C/G2-130[»]
1P3OX-ray2.75C/G2-130[»]
1P3PX-ray2.70C/G2-130[»]
1S32X-ray2.05C/G2-120[»]
1ZBBX-ray9.00C/G/c/g2-130[»]
1ZLAX-ray2.90C/G2-130[»]
2FJ7X-ray3.20C/G2-130[»]
2NZDX-ray2.65C/G2-120[»]
3B6FX-ray3.45C/G2-130[»]
3B6GX-ray3.45C/G2-130[»]
3C1BX-ray2.20C/G2-130[»]
3C1CX-ray3.15C/G2-130[»]
3KUYX-ray2.90C/G2-120[»]
3KWQX-ray3.50C/G15-121[»]
3LJAX-ray2.75C/G2-130[»]
3MNNX-ray2.50C/G2-120[»]
3O62X-ray3.22C/G2-130[»]
3REHX-ray2.50C/G2-130[»]
3REIX-ray2.65C/G2-130[»]
3REJX-ray2.55C/G2-130[»]
3REKX-ray2.60C/G2-130[»]
3RELX-ray2.70C/G2-130[»]
3TU4X-ray3.00C/G2-130[»]
3UT9X-ray2.20C/G2-130[»]
3UTAX-ray2.07C/G2-130[»]
3UTBX-ray2.20C/G2-130[»]
4J8UX-ray2.38C/G2-130[»]
4J8VX-ray2.58C/G2-130[»]
4J8WX-ray2.41C/G2-130[»]
4J8XX-ray2.87C/G2-130[»]
4LD9X-ray3.31C/G1-130[»]
4R8PX-ray3.28C/G2-130[»]
4WU8X-ray2.45C/G2-130[»]
4WU9X-ray2.60C/G2-130[»]
4XUJX-ray3.18C/G2-130[»]
4XZQX-ray2.40C/G15-121[»]
4YS3X-ray3.00C/G15-121[»]
4Z66X-ray2.50C/G15-121[»]
4ZUXX-ray3.82C/G/M/Q1-130[»]
5CP6X-ray2.60C/G2-130[»]
5DNMX-ray2.81C/G2-130[»]
5DNNX-ray2.80C/G2-130[»]
5E5AX-ray2.81C/G1-130[»]
5F99X-ray2.63C/G2-130[»]
5G2EX-ray6.70C/G/K/O/S/W14-119[»]
5HQ2X-ray4.50G2-130[»]
5MLUX-ray2.80C/G15-119[»]
5NL0X-ray5.40C/G/M2-130[»]
5O9Gelectron microscopy4.80C/G1-130[»]
5OMXX-ray2.32C/G2-130[»]
5ONGX-ray2.80C/G2-130[»]
5ONWX-ray2.80C/G2-130[»]
5OXVX-ray6.72C/G/M/Q1-130[»]
5OY7X-ray5.77C/G/K/O/S/W/a/e1-130[»]
5X0Xelectron microscopy3.97C/G1-130[»]
5X0Yelectron microscopy4.69C/G2-130[»]
5XF6X-ray2.63C/G2-130[»]
6FTXelectron microscopy4.50C/G1-130[»]
6G0Lelectron microscopy4.50C/G1-130[»]
ProteinModelPortaliP06897
SMRiP06897
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi592527, 2 interactors
DIPiDIP-39144N
IntActiP06897, 10 interactors

Proteomic databases

PRIDEiP06897

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi734746
KEGGixla:734746

Organism-specific databases

CTDi734746
XenbaseiXB-GENE-6493983 h2afx

Phylogenomic databases

HOVERGENiHBG009342
KOiK11251

Miscellaneous databases

EvolutionaryTraceiP06897

Family and domain databases

CDDicd00074 H2A, 1 hit
Gene3Di1.10.20.10, 1 hit
InterProiView protein in InterPro
IPR009072 Histone-fold
IPR002119 Histone_H2A
IPR007125 Histone_H2A/H2B/H3
IPR032454 Histone_H2A_C
IPR032458 Histone_H2A_CS
PfamiView protein in Pfam
PF00125 Histone, 1 hit
PF16211 Histone_H2A_C, 1 hit
PRINTSiPR00620 HISTONEH2A
SMARTiView protein in SMART
SM00414 H2A, 1 hit
SUPFAMiSSF47113 SSF47113, 1 hit
PROSITEiView protein in PROSITE
PS00046 HISTONE_H2A, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiH2A1_XENLA
AccessioniPrimary (citable) accession number: P06897
Secondary accession number(s): Q3B8I8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: October 10, 2018
This is version 137 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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